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PDBsum entry 1sce
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protein metals Protein-protein interface(s) links
Cell cycle regulatory protein PDB id
1sce

 

 

 

 

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Contents
Protein chains
97 a.a. *
111 a.a. *
103 a.a. *
Metals
_CL ×3
Waters ×238
* Residue conservation analysis
PDB id:
1sce
Name: Cell cycle regulatory protein
Title: Crystal structure of the cell cycle regulatory protein suc1 reveals a novel beta-hinge conformational switch
Structure: Suc1. Chain: a, b, c, d. Engineered: yes
Source: Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Tetramer (from PQS)
Resolution:
2.20Å     R-factor:   0.193     R-free:   0.284
Authors: Y.Bourne,J.A.Tainer
Key ref: Y.Bourne et al. (1995). Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch. Proc Natl Acad Sci U S A, 92, 10232-10236. PubMed id: 7479758 DOI: 10.1073/pnas.92.22.10232
Date:
11-May-95     Release date:   29-Jan-96    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08463  (CKS1_SCHPO) -  Cyclin-dependent kinases regulatory subunit from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc: 		113 a.a.
97 a.a.
Protein chain
Pfam   ArchSchema ?
P08463  (CKS1_SCHPO) -  Cyclin-dependent kinases regulatory subunit from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc: 		113 a.a.
111 a.a.
Protein chain
Pfam   ArchSchema ?
P08463  (CKS1_SCHPO) -  Cyclin-dependent kinases regulatory subunit from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc: 		113 a.a.
103 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1073/pnas.92.22.10232 Proc Natl Acad Sci U S A 92:10232-10236 (1995)
PubMed id: 7479758  
 
 
Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.
Y.Bourne, A.S.Arvai, S.L.Bernstein, M.H.Watson, S.I.Reed, J.E.Endicott, M.E.Noble, L.N.Johnson, J.A.Tainer.
 
  ABSTRACT  
 
The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer. Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits. This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here. This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs to the family of domain-swapping proteins, consisting of intertwined and dimeric protein structures in which the dual assembly modes regulate their function.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19768682 J.Luo, A.Teplyakov, G.Obmolova, T.Malia, S.J.Wu, E.Beil, A.Baker, B.Swencki-Underwood, Y.Zhao, J.Sprenkle, K.Dixon, R.Sweet, and G.L.Gilliland (2009).
Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-strand swapping.
  Proteins, 77, 1009-1014.
PDB codes: 3i84 3i85
19137579 S.Rodziewicz-Motowidło, J.Iwaszkiewicz, R.Sosnowska, P.Czaplewska, E.Sobolewski, A.Szymańska, K.Stachowiak, and A.Liwo (2009).
The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants.
  Biopolymers, 91, 373-383.  
18078545 C.D.Putnam, M.Hammel, G.L.Hura, and J.A.Tainer (2007).
X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution.
  Q Rev Biophys, 40, 191-285.  
17892493 G.Lippens, I.Landrieu, and C.Smet (2007).
Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.
  FEBS J, 274, 5211-5222.  
15843986 J.A.Kelly, E.A.Williams, and M.C.Wilce (2005).
Preliminary crystallographic analysis of the Cks protein p13(suc1P90AP92A) from Schizosacharromyces pombe.
  Eur Biophys J, 34, 430-433.  
12623012 F.Rousseau, J.W.Schymkowitz, and L.S.Itzhaki (2003).
The unfolding story of three-dimensional domain swapping.
  Structure, 11, 243-251.  
12015148 F.Rousseau, J.W.Schymkowitz, H.R.Wilkinson, and L.S.Itzhaki (2002).
The structure of the transition state for folding of domain-swapped dimeric p13suc1.
  Structure, 10, 649-657.  
11839489 M.E.Newcomer (2002).
Protein folding and three-dimensional domain swapping: a strained relationship?
  Curr Opin Struct Biol, 12, 48-53.  
12005431 S.T.Arold, M.K.Hoellerer, and M.E.Noble (2002).
The structural basis of localization and signaling by the focal adhesion targeting domain.
  Structure, 10, 319-327.
PDB codes: 1k04 1k05
11180561 A.P.Demchenko (2001).
Recognition between flexible protein molecules: induced and assisted folding.
  J Mol Recognit, 14, 42-61.  
11344301 F.Rousseau, J.W.Schymkowitz, H.R.Wilkinson, and L.S.Itzhaki (2001).
Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues.
  Proc Natl Acad Sci U S A, 98, 5596-5601.  
11573096 J.W.Schymkowitz, F.Rousseau, H.R.Wilkinson, A.Friedler, and L.S.Itzhaki (2001).
Observation of signal transduction in three-dimensional domain swapping.
  Nat Struct Biol, 8, 888-892.  
10673427 D.O.Alonso, E.Alm, and V.Daggett (2000).
Characterization of the unfolding pathway of the cell-cycle protein p13suc1 by molecular dynamics simulations: implications for domain swapping.
  Structure, 8, 101-110.  
10673431 J.W.Schymkowitz, F.Rousseau, L.R.Irvine, and L.S.Itzhaki (2000).
The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping.
  Structure, 8, 89.  
10997903 Y.Bourne, M.H.Watson, A.S.Arvai, S.L.Bernstein, S.I.Reed, and J.A.Tainer (2000).
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.
  Structure, 8, 841-850.
PDB code: 1qb3
10607671 J.A.Endicott, M.E.Noble, and J.A.Tucker (1999).
Cyclin-dependent kinases: inhibition and substrate recognition.
  Curr Opin Struct Biol, 9, 738-744.  
9671502 A.P.Saint-Jean, K.R.Phillips, D.J.Creighton, and M.J.Stone (1998).
Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping.
  Biochemistry, 37, 10345-10353.  
  9541384 D.Xu, C.J.Tsai, and R.Nussinov (1998).
Mechanism and evolution of protein dimerization.
  Protein Sci, 7, 533-544.  
  9632748 E.A.Egan, and M.J.Solomon (1998).
Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.
  Mol Cell Biol, 18, 3659-3667.  
9760264 M.C.Morris, F.Heitz, and G.Divita (1998).
Kinetics of dimerization and interactions of p13suc1 with cyclin-dependent kinases.
  Biochemistry, 37, 14257-14266.  
  9841670 M.D.Mendenhall, and A.E.Hodge (1998).
Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.
  Microbiol Mol Biol Rev, 62, 1191-1243.  
  9311818 A.Pujol, L.Deleu, J.P.Nüesch, C.Cziepluch, J.C.Jauniaux, and J.Rommelaere (1997).
Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1.
  J Virol, 71, 7393-7403.  
8939669 D.O.Morgan (1996).
The dynamics of cyclin dependent kinase structure.
  Curr Opin Cell Biol, 8, 767-772.  
8939596 J.Pines (1996).
Cell cycle: reaching for a role for the Cks proteins.
  Curr Biol, 6, 1399-1402.  
8805536 N.Khazanovich, K.Bateman, M.Chernaia, M.Michalak, and M.James (1996).
Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer.
  Structure, 4, 299-309.
PDB code: 1puc
8601310 Y.Bourne, M.H.Watson, M.J.Hickey, W.Holmes, W.Rocque, S.I.Reed, and J.A.Tainer (1996).
Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.
  Cell, 84, 863-874.
PDB code: 1buh
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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